A0A7S0R2N4 · A0A7S0R2N4_9CHLO

Function

function

Bifunctional aspartate kinase and homoserine dehydrogenase that catalyzes the first and the third steps toward the synthesis of lysine, methionine and threonine from aspartate.

Catalytic activity

Cofactor

a metal cation (UniProtKB | Rhea| CHEBI:25213 )

Pathway

Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3.
Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5.

GO annotations

AspectTerm
Molecular Functionaspartate kinase activity
Molecular FunctionATP binding
Molecular Functionhomoserine dehydrogenase activity
Molecular Functionmetal ion binding
Molecular FunctionNADP binding
Biological Processhomoserine biosynthetic process
Biological Processlysine biosynthetic process via diaminopimelate
Biological Processmethionine biosynthetic process
Biological Processphosphorylation
Biological Processthreonine biosynthetic process

Keywords

Enzyme and pathway databases

    • UPA00034UER00015
    • UPA00050UER00063
    • UPA00051UER00462

Names & Taxonomy

Protein names

  • Recommended name
    ACT domain-containing protein

Gene names

    • ORF names
      CLEI1391_LOCUS1338

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • SAG 11-49
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Chlorophyta > core chlorophytes > Chlorophyceae > CS clade > Chlamydomonadales > Chlamydomonadaceae > Chlamydomonas

Accessions

  • Primary accession
    A0A7S0R2N4

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias47-76Polar residues
Region47-77Disordered
Domain435-510ACT
Domain516-593ACT

Sequence similarities

In the C-terminal section; belongs to the homoserine dehydrogenase family.
In the N-terminal section; belongs to the aspartokinase family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    939
  • Mass (Da)
    100,661
  • Last updated
    2021-06-02 v1
  • Checksum
    C449F2BCC9823287
AGTAQASTSITMMLKAGSGLGSARQGTAKSTLAQCLNVVPRAVHGQDMSSQTRISPVSTCNPTSAAPISRSAQRRQRMPVQAVVMQSDRANTGDGFKRGSHWQVHKFGGTCMAAAERIKAVAELMIKENNQGTVVVVSAMGSHPSSPLKVTDVILNMIQKAAKQDQAFLLDLAALQDKHVETAKALLGQTPELTSFVSRLLDDMANLKAMLQAMSIAGMSTEAFADYVVGHGELWSAQLLTLCCQQLGADAVFMDTRDVLVVVPTSDGTSVDLVEDVSNARMDDWFKRNGNHKIVVATGFIAKNKEGQATTLKRNGSDFSATIMGSLFKAGHITIWTDVDGVYSADPRKVPEAVCLPSMTYHEAWELSYFGANVLHPRTTLPAMKYHIPITIRNFFNLPSKGTVVSDFESDQAVYQGKNTVKGLATIDHTTLINVEGTGMVGVPGIASAIFSTVRDAGINVIMISQASSEQSICFAVKAADGDAAVRVLQRRFADAIASGRVSAVQAIPNCCVLAVVGQGMVSKRGVAATLFSALAKANVNIKAMAQGSSEYNITVLIDQVDSERALRAVHSRFYLSSTPIGIGLVGPGLIGGALLDQLREQAETLRAEFAIDLRILGISTSKQMVLSEKGVDMSRWRDEFKEKGQPVDLAKFGDHLANSYIPNRAIVDCTASDAPAQMYLPWMKQGIHIITPNKKLGSGPLELYNQVKKVGRESYIHFFYEGTVGAGLPVMGTLKHLVETGDKVQRIEGIFSGTLSYIFNTWGSDARKFSEIVSDAKAKGFTEPDPRDDLNGTDVARKVAILARECGLQLELSDIPVESLVPEPLRAIPDSATYMARLPEFDGDMAARLKEAQDAGEVLRFVGVVDVAGGKGSVELRRYPKTHPFAQLSGSDNIIAFTTKRYTKQPLIVRGPGAGADVTAGGVFSDLLKLAAYLGAPS

Features

Showing features for non-terminal residue, compositional bias.

Type
IDPosition(s)Description
Non-terminal residue1
Compositional bias47-76Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
HBFB01002601
EMBL· GenBank· DDBJ
CAD8665337.1
EMBL· GenBank· DDBJ
Transcribed RNA

Similar Proteins

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